PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21210672-2 2011 At room temperature, the native structure of cytochrome c is maintained in relatively high ionic liquid concentrations (50-70% AAF/water or AAF/phosphate buffer pH 7.0) in contrast with denaturation of cytochrome c in similar solutions of methanol or acetonitrile with water or buffer cosolvents. Methanol 239-247 cytochrome c, somatic Homo sapiens 45-57 21210672-4 2011 About one-third of the enzyme activity of cytochrome c in 80% AAF-20% water can be maintained as compared with phosphate buffer, and this is greater than the activities measured in corresponding methanol and acetonitrile aqueous solutions. Methanol 195-203 cytochrome c, somatic Homo sapiens 42-54 21783700-8 2006 The results show the typical ladder profile of oligonucleosomal fragments characteristics of apoptosis and the secreted cytosolic cytochrome c level was increased by treatment of methanol fraction of UD. Methanol 179-187 cytochrome c, somatic Homo sapiens 130-142 20683519-0 2010 Reversible conformational change of cytochrome c at a modified gold electrode in methanol. Methanol 81-89 cytochrome c, somatic Homo sapiens 36-48 20683519-1 2010 Changes in the secondary structure of cytochrome c on immersion in methanol were monitored using circular dichroism. Methanol 67-75 cytochrome c, somatic Homo sapiens 38-50 19283282-0 2009 Reversible increase in the redox potential of cytochrome c in methanol. Methanol 62-70 cytochrome c, somatic Homo sapiens 46-58 19283282-1 2009 The E degrees " of cytochrome c on a self-assembled monolayer (SAM) modified gold electrode increased by 300 mV immediately on immersion in methanol; on re-immersion of the electrode in aqueous buffer, the original faradaic response was restored, but over a period of 120 min, indicating that methanol causes a significant change in conformation/orientation of the protein. Methanol 140-148 cytochrome c, somatic Homo sapiens 19-31 19283282-1 2009 The E degrees " of cytochrome c on a self-assembled monolayer (SAM) modified gold electrode increased by 300 mV immediately on immersion in methanol; on re-immersion of the electrode in aqueous buffer, the original faradaic response was restored, but over a period of 120 min, indicating that methanol causes a significant change in conformation/orientation of the protein. Methanol 293-301 cytochrome c, somatic Homo sapiens 19-31 15667182-2 2005 In this study, we investigate the electrochemical response of cytochrome c in aqueous/organic solvent mixtures (100% aqueous buffer, 30% acetonitrile, 40% dimethyl sulfoxide, and 50% methanol), reporting the redox potential (E degrees"), enthalpy, and entropy of reduction. Methanol 183-191 cytochrome c, somatic Homo sapiens 62-74 11281607-0 2001 The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry. Methanol 4-12 cytochrome c, somatic Homo sapiens 71-83 11281607-1 2001 The methanol-induced conformational transitions under acidic conditions for beta-lactoglobulin, cytochrome c, and ubiquitin, representing three different classes of proteins with beta-sheets, alpha-helices, and both alpha-helices and beta-sheets, respectively, are studied under equilibrium conditions by electrospray ionization mass spectrometry (ESI-MS). Methanol 4-12 cytochrome c, somatic Homo sapiens 96-108 11073261-2 2000 The charge state distributions of cytochrome c and myoglobin, formed from 47%/50%/3% water/solvent/acetic acid solutions, shift to lower charge (higher m/z) when the 50% solvent fraction is changed from water to methanol, to acetonitrile, to isopropanol. Methanol 212-220 cytochrome c, somatic Homo sapiens 34-46 8676385-0 1996 The methanol-induced globular and expanded denatured states of cytochrome c: a study by CD fluorescence, NMR and small-angle X-ray scattering. Methanol 4-12 cytochrome c, somatic Homo sapiens 63-75 11671080-8 1999 The width of an empty cavity of Co(C6[16]Cyc) shrinks by 0.3 A in methanol solution, as compared to vacuum simulations. Methanol 66-74 cytochrome c, somatic Homo sapiens 41-44 11196900-0 2000 Supramolecular complex of cytochrome c with lariat ether: solubilization, redox behavior and catalytic activity of cytochrome c in methanol. Methanol 131-139 cytochrome c, somatic Homo sapiens 26-38 11196900-0 2000 Supramolecular complex of cytochrome c with lariat ether: solubilization, redox behavior and catalytic activity of cytochrome c in methanol. Methanol 131-139 cytochrome c, somatic Homo sapiens 115-127 11196900-1 2000 A variety of lariat ethers were employed to solubilize water-soluble cytochrome c in methanol, in which alcohol, ether, ester, amine, and amide functionalities were attached as cation-ligating side arms to 18-crown-6, 15-crown-5, and 12-crown-4 rings. Methanol 85-93 cytochrome c, somatic Homo sapiens 69-81 11196900-3 2000 The resulting cytochrome c-lariat ether complexes were electrochemically and spectroscopically characterized and confirmed to have redox-active heme structures of 6-coordinate low-spin population in methanol. Methanol 199-207 cytochrome c, somatic Homo sapiens 14-26 11196900-4 2000 Some of them catalyzed the oxidation of pinacyanol chloride with hydrogen peroxide in methanol and exhibited higher activities than unmodified cytochrome c and its poly(ethylene glycolated) derivative. Methanol 86-94 cytochrome c, somatic Homo sapiens 143-155 9315869-0 1997 Acid-induced unfolding of cytochrome c at different methanol concentrations: electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure. Methanol 52-60 cytochrome c, somatic Homo sapiens 26-38 8676385-1 1996 Methanol-induced conformational transitions of cytochrome c(cyt c) at acidic pH values were investigated with a combined use of far and near-UV CD, fluorescence, NMR spectroscopy and small-angle X-ray scattering. Methanol 0-8 cytochrome c, somatic Homo sapiens 47-59 1329094-1 1992 Temperature dependence of the thermodynamics of folding/unfolding for cytochrome c has been determined as a function of moderate [0-10% (vol/vol)] concentrations of methanol. Methanol 165-173 cytochrome c, somatic Homo sapiens 70-82 8634247-1 1996 Methanol-induced conformational transitions in cytochrome c have been studied by near- and far-UV circular dichroism, Trp fluorescence, microcalorimetry, and diffusion measurements. Methanol 0-8 cytochrome c, somatic Homo sapiens 47-59 3031209-3 1987 The monomeric heme octapeptide from cytochrome c, microperoxidase-8, (MP-8), coordinates CN- with log K = 7.55 +/- 0.04 at 25 degrees C in 20% (v/v) aqueous methanol. Methanol 157-165 cytochrome c, somatic Homo sapiens 36-48 32922-0 1978 [Spectral parameters of the cytochrome c and hemoglobin interaction with methanol and aniline]. Methanol 73-81 cytochrome c, somatic Homo sapiens 28-40 32922-1 1978 At 20 degrees C, in a phosphate buffer, pH 5,8--8,0, methanol and aniline interactions with hemoglobin and cytochrome c were studied using the difference spectrophotometry method. Methanol 53-61 cytochrome c, somatic Homo sapiens 107-119 31522674-9 2019 These changes were reversible, which corroborates the conclusion on the CytC transition to the molten globule conformation in methanol-containing solutions. Methanol 126-134 cytochrome c, somatic Homo sapiens 72-76 23526115-3 2012 Experiments with cytochrome c (Cytc) demonstrated that methanol induced conformational shifts previously observed with ESI are also easily observed with liquid DESI. Methanol 55-63 cytochrome c, somatic Homo sapiens 17-29 24354363-3 2014 Equilibrium unfolding of differently charged cytochrome c molecules in water-methanol binary mixtures, where the alcohol acts as the cosolvent denaturant, was used to quantify the preferential exclusion of water during the unfolding transition. Methanol 77-85 cytochrome c, somatic Homo sapiens 45-57 29856995-9 2018 In methanol-water phase, CL and CL + CytC mixture form particles of 83.7 +- 9.8 and 71.3 +- 11.6 nm, respectively. Methanol 3-11 cytochrome c, somatic Homo sapiens 37-41 28735170-4 2017 Therefore, atomistic molecular dynamics (MD) simulations have been carried out to investigate the effect of different solvents (water, urea/water, MeOH and DMSO) on the structure and conformations of apoptotic cyt-c (Fe3+). Methanol 147-151 cytochrome c, somatic Homo sapiens 210-215 28735170-11 2017 Essential dynamics analysis implies that the overall motions of cyt-c in water, MeOH and urea/water are involved in three to four eigenvectors and in first eigenvector in DMSO. Methanol 80-84 cytochrome c, somatic Homo sapiens 64-69 26421324-2 2015 In aqueous solution, 2-thiophenone and 4-hydroxymethyl-1,3-dioxolan-2-one (HD) at a concentration of 2% by volume can increase the average charge of cytochrome c and myoglobin by up to 163%, resulting in even higher charge states than those that are produced from water/methanol/acid solutions in which these proteins are denatured. Methanol 270-278 cytochrome c, somatic Homo sapiens 149-161 22246045-6 2012 By mixing water with methanol, a refolding of cytochrome C is observed as the water percentage increases in the plume due to the preponderant evaporation of volatile methanol. Methanol 21-29 cytochrome c, somatic Homo sapiens 46-58 22246045-6 2012 By mixing water with methanol, a refolding of cytochrome C is observed as the water percentage increases in the plume due to the preponderant evaporation of volatile methanol. Methanol 166-174 cytochrome c, somatic Homo sapiens 46-58 22056335-7 2012 Increased levels of Bax and cytosolic cytochrome C and decreased levels of Bcl2 were also observed in MeOH:water (80:20) treated MCF-7 cells. Methanol 102-106 cytochrome c, somatic Homo sapiens 38-50